| content |
HEADER HYDROLASE 20-NOV-13 4CG3
TITLE STRUCTURAL AND FUNCTIONAL STUDIES ON A THERMOSTABLE POLYETHYLENE
TITLE 2 THEREPHTALATE DEGRADING HYDROLASE FROM THERMOBIFIDA FUSCA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.74;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA;
SOURCE 3 ORGANISM_TAXID: 2021;
SOURCE 4 STRAIN: KW3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, PET DEGRADATION, ALPHA-BETA- FOLD
EXPDTA X-RAY DIFFRACTION
NUMMDL 77
AUTHOR C.ROTH,R.WEI,T.OESER,J.THEN,C.FOELLNER,W.ZIMMERMANN,N.STRAETER
REVDAT 1 25-JUN-14 4CG3 0
JRNL AUTH C.ROTH,R.WEI,T.OESER,J.THEN,C.FOLLNER,W.ZIMMERMANN,N.STRATER
JRNL TITL STRUCTURAL AND FUNCTIONAL STUDIES ON A THERMOSTABLE
JRNL TITL 2 POLYETHYLENE TEREPHTHALATE DEGRADING HYDROLASE FROM
JRNL TITL 3 THERMOBIFIDA FUSCA.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. 2014
JRNL REFN ESSN 1432-0614
JRNL PMID 24728714
JRNL DOI 10.1007/S00253-014-5672-0
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.122
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.24
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.93
REMARK 3 NUMBER OF REFLECTIONS : 36710
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1202
REMARK 3 R VALUE (WORKING SET) : 0.1173
REMARK 3 FREE R VALUE : 0.1492
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.9
REMARK 3 FREE R VALUE TEST SET COUNT : 3279
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 23.1247 - 4.3984 0.99 1524 150 0.1223 0.1271
REMARK 3 2 4.3984 - 3.4950 1.00 1519 127 0.1069 0.1350
REMARK 3 3 3.4950 - 3.0544 1.00 1431 166 0.1202 0.1527
REMARK 3 4 3.0544 - 2.7756 1.00 1478 137 0.1241 0.1500
REMARK 3 5 2.7756 - 2.5769 1.00 1453 151 0.1137 0.1434
REMARK 3 6 2.5769 - 2.4252 1.00 1441 140 0.1029 0.1174
REMARK 3 7 2.4252 - 2.3038 1.00 1482 129 0.1021 0.1388
REMARK 3 8 2.3038 - 2.2036 1.00 1442 161 0.0995 0.1364
REMARK 3 9 2.2036 - 2.1189 1.00 1455 147 0.0976 0.1422
REMARK 3 10 2.1189 - 2.0458 1.00 1449 144 0.1009 0.1384
REMARK 3 11 2.0458 - 1.9819 1.00 1429 144 0.1000 0.1460
REMARK 3 12 1.9819 - 1.9252 1.00 1425 163 0.1014 0.1574
REMARK 3 13 1.9252 - 1.8746 1.00 1464 126 0.1113 0.1384
REMARK 3 14 1.8746 - 1.8289 1.00 1460 146 0.1193 0.1638
REMARK 3 15 1.8289 - 1.7873 1.00 1439 127 0.1314 0.1670
REMARK 3 16 1.7873 - 1.7493 1.00 1429 138 0.1419 0.1723
REMARK 3 17 1.7493 - 1.7143 1.00 1461 134 0.1446 0.2002
REMARK 3 18 1.7143 - 1.6820 1.00 1450 154 0.1504 0.1927
REMARK 3 19 1.6820 - 1.6519 1.00 1439 142 0.1503 0.2091
REMARK 3 20 1.6519 - 1.6239 1.00 1423 145 0.1575 0.2032
REMARK 3 21 1.6239 - 1.5978 1.00 1466 131 0.1565 0.2078
REMARK 3 22 1.5978 - 1.5732 1.00 1421 133 0.1805 0.2174
REMARK 3 23 1.5732 - 1.5500 1.00 1451 144 0.1935 0.2583
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.11
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.59
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINED USING PHENIX.ENSEMBLE REFINEMENT
REMARK 4
REMARK 4 4CG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-DEC-13.
REMARK 100 THE PDBE ID CODE IS EBI-59014.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.541
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36710
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.55
REMARK 200 RESOLUTION RANGE LOW (A) : 23.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.55
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.8
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.7
REMARK 200 R MERGE FOR SHELL (I) : 0.59
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1JFR
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 58.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 58.95000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.22000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 9.11000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.95000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.33000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.95000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.95000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 18.22000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 58.95000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 27.33000
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 58.95000
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 9.11000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 1 MET A -30
REMARK 465 1 LYS A -29
REMARK 465 1 TYR A -28
REMARK 465 1 LEU A -27
REMARK 465 1 LEU A -26
REMARK 465 1 PRO A -25
REMARK 465 1 THR A -24
REMARK 465 1 ALA A -23
REMARK 465 1 ALA A -22
REMARK 465 1 ALA A -21
REMARK 465 1 GLY A -20
REMARK 465 1 LEU A -19
REMARK 465 1 LEU A -18
REMARK 465 1 LEU A -17
REMARK 465 1 LEU A -16
REMARK 465 1 ALA A -15
REMARK 465 1 ALA A -14
REMARK 465 1 GLN A -13
REMARK 465 1 PRO A -12
REMARK 465 1 ALA A -11
REMARK 465 1 MET A -10
REMARK 465 1 ALA A -9
REMARK 465 1 MET A -8
REMARK 465 1 ASP A -7
REMARK 465 1 ILE A -6
REMARK 465 1 GLY A -5
REMARK 465 1 ILE A -4
REMARK 465 1 ASN A -3
REMARK 465 1 SER A -2
REMARK 465 1 ASP A -1
REMARK 465 1 PRO A 0
REMARK 465 1 ASN A 264
REMARK 465 1 SER A 265
REMARK 465 1 SER A 266
REMARK 465 1 SER A 267
REMARK 465 1 VAL A 268
REMARK 465 1 ASP A 269
REMARK 465 1 LYS A 270
REMARK 465 1 LEU A 271
REMARK 465 1 ALA A 272
REMARK 465 1 ALA A 273
REMARK 465 1 ALA A 274
REMARK 465 1 LEU A 275
REMARK 465 1 GLU A 276
REMARK 465 1 HIS A 277
REMARK 465 1 HIS A 278
REMARK 465 1 HIS A 279
REMARK 465 1 HIS A 280
REMARK 465 1 HIS A 281
REMARK 465 1 HIS A 282
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 121 O HOH A 1196 2.13
REMARK 500 OG SER A 130 O HOH A 1105 2.13
REMARK 500 O PHE A 209 N ILE A 213 2.08
REMARK 500 O PHE A 209 H ILE A 213 1.50
REMARK 500 O LEU A 248 N VAL A 252 2.15
REMARK 500 O LEU A 248 H VAL A 252 1.45
REMARK 500 O HOH A 1167 O HOH A 1179 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1121 O HOH A 1151 7554 1.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 26 CG GLU A 26 CD 0.090
REMARK 500 2 ARG A 31 CB ARG A 31 CG 0.176
REMARK 500 2 ASP A 94 CB ASP A 94 CG 0.139
REMARK 500 2 MET A 127 CB MET A 127 CG -0.267
REMARK 500 2 MET A 127 CG MET A 127 SD -0.173
REMARK 500 4 MET A 127 CB MET A 127 CG 0.208
REMARK 500 5 MET A 127 CB MET A 127 CG 0.237
REMARK 500 5 GLU A 253 CB GLU A 253 CG 0.144
REMARK 500 7 VAL A 54 CB VAL A 54 CG1 -0.128
REMARK 500 8 ASP A 85 CB ASP A 85 CG -0.135
REMARK 500 10 MET A 131 CG MET A 131 SD -0.176
REMARK 500 11 GLU A 5 CB GLU A 5 CG 0.153
REMARK 500 11 GLU A 5 CG GLU A 5 CD 0.105
REMARK 500 11 MET A 127 CB MET A 127 CG 0.252
REMARK 500 14 MET A 127 CG MET A 127 SD -0.158
REMARK 500 14 MET A 131 CB MET A 131 CG 0.378
REMARK 500 15 MET A 131 CB MET A 131 CG 0.211
REMARK 500 16 ARG A 138 CG ARG A 138 CD -0.169
REMARK 500 17 MET A 131 CG MET A 131 SD 0.173
REMARK 500 18 ALA A 53 CA ALA A 53 CB -0.131
REMARK 500 20 SER A 117 CB SER A 117 OG -0.097
REMARK 500 20 MET A 131 CB MET A 131 CG 0.483
REMARK 500 20 MET A 131 CG MET A 131 SD 0.163
REMARK 500 21 ARG A 116 CB ARG A 116 CG -0.206
REMARK 500 23 GLU A 26 CB GLU A 26 CG 0.121
REMARK 500 24 GLU A 26 CB GLU A 26 CG 0.132
REMARK 500 24 GLU A 26 CG GLU A 26 CD 0.094
REMARK 500 24 ASN A 48 CB ASN A 48 CG 0.155
REMARK 500 25 ASN A 48 CB ASN A 48 CG 0.151
REMARK 500 27 GLU A 72 CB GLU A 72 CG 0.131
REMARK 500 27 MET A 107 CG MET A 107 SD 0.180
REMARK 500 29 TYR A 43 CB TYR A 43 CG -0.098
REMARK 500 29 TYR A 43 CD1 TYR A 43 CE1 -0.096
REMARK 500 30 ARG A 46 CB ARG A 46 CG -0.180
REMARK 500 30 SER A 122 CB SER A 122 OG -0.093
REMARK 500 37 VAL A 115 CB VAL A 115 CG1 -0.188
REMARK 500 39 ASN A 28 CB ASN A 28 CG 0.203
REMARK 500 39 ARG A 73 CB ARG A 73 CG -0.172
REMARK 500 39 GLU A 254 CG GLU A 254 CD 0.090
REMARK 500 40 GLU A 98 CB GLU A 98 CG -0.117
REMARK 500 40 ARG A 143 C ARG A 143 O 0.128
REMARK 500 41 GLU A 72 CG GLU A 72 CD 0.093
REMARK 500 41 ARG A 143 C ARG A 143 O 0.137
REMARK 500 43 ARG A 110 CB ARG A 110 CG 0.169
REMARK 500 43 ARG A 110 CG ARG A 110 CD 0.227
REMARK 500 44 PRO A 144 CA PRO A 144 C -0.169
REMARK 500 46 ARG A 31 CB ARG A 31 CG 0.182
REMARK 500 48 ASN A 48 CB ASN A 48 CG 0.157
REMARK 500 48 TYR A 262 CB TYR A 262 CG 0.112
REMARK 500 49 ARG A 31 CB ARG A 31 CG 0.179
REMARK 500
REMARK 500 THIS ENTRY HAS 75 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 1 ARG A 31 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 1 THR A 63 CB - CA - C ANGL. DEV. = -17.5 DEGREES
REMARK 500 1 ASP A 94 CB - CG - OD1 ANGL. DEV. = 10.5 DEGREES
REMARK 500 1 ASP A 94 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 1 MET A 127 CG - SD - CE ANGL. DEV. = -11.7 DEGREES
REMARK 500 1 PRO A 214 C - N - CA ANGL. DEV. = 15.7 DEGREES
REMARK 500 1 PRO A 214 C - N - CD ANGL. DEV. = -12.7 DEGREES
REMARK 500 1 PRO A 214 N - CA - C ANGL. DEV. = 18.2 DEGREES
REMARK 500 1 ASN A 215 N - CA - C ANGL. DEV. = 17.8 DEGREES
REMARK 500 1 GLY A 243 N - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 2 SER A 25 N - CA - CB ANGL. DEV. = 9.3 DEGREES
REMARK 500 2 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 31 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 2 GLY A 62 N - CA - C ANGL. DEV. = 19.1 DEGREES
REMARK 500 2 ASP A 94 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 2 MET A 127 CB - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 2 MET A 127 CG - SD - CE ANGL. DEV. = -17.4 DEGREES
REMARK 500 2 PRO A 214 C - N - CA ANGL. DEV. = 22.2 DEGREES
REMARK 500 2 PRO A 214 C - N - CD ANGL. DEV. = -20.3 DEGREES
REMARK 500 2 PRO A 214 CB - CA - C ANGL. DEV. = -14.9 DEGREES
REMARK 500 2 GLY A 243 N - CA - C ANGL. DEV. = -23.5 DEGREES
REMARK 500 2 PRO A 263 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 2 PRO A 263 C - N - CD ANGL. DEV. = -14.0 DEGREES
REMARK 500 3 MET A 127 CG - SD - CE ANGL. DEV. = -22.1 DEGREES
REMARK 500 3 GLY A 243 N - CA - C ANGL. DEV. = -22.0 DEGREES
REMARK 500 4 ASP A 12 CB - CG - OD2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 4 SER A 66 CB - CA - C ANGL. DEV. = -13.3 DEGREES
REMARK 500 4 MET A 107 CB - CG - SD ANGL. DEV. = -26.0 DEGREES
REMARK 500 4 MET A 107 CG - SD - CE ANGL. DEV. = -15.0 DEGREES
REMARK 500 4 MET A 127 CG - SD - CE ANGL. DEV. = -26.8 DEGREES
REMARK 500 4 PRO A 244 C - N - CA ANGL. DEV. = 18.9 DEGREES
REMARK 500 4 PRO A 244 CA - N - CD ANGL. DEV. = -9.0 DEGREES
REMARK 500 4 GLY A 247 N - CA - C ANGL. DEV. = 15.2 DEGREES
REMARK 500 4 LEU A 248 N - CA - C ANGL. DEV. = -20.2 DEGREES
REMARK 500 4 PRO A 263 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 5 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 5 MET A 127 CA - CB - CG ANGL. DEV. = 11.5 DEGREES
REMARK 500 5 MET A 127 CG - SD - CE ANGL. DEV. = -12.4 DEGREES
REMARK 500 5 PRO A 244 C - N - CA ANGL. DEV. = 54.4 DEGREES
REMARK 500 5 PRO A 244 C - N - CD ANGL. DEV. = -52.8 DEGREES
REMARK 500 6 THR A 11 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 6 ARG A 46 CG - CD - NE ANGL. DEV. = 13.1 DEGREES
REMARK 500 6 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 6 MET A 127 CB - CG - SD ANGL. DEV. = -30.3 DEGREES
REMARK 500 6 PRO A 244 C - N - CA ANGL. DEV. = 56.9 DEGREES
REMARK 500 6 PRO A 244 C - N - CD ANGL. DEV. = -56.7 DEGREES
REMARK 500 6 ARG A 245 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 7 ASP A 12 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 7 MET A 127 CG - SD - CE ANGL. DEV. = -12.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 375 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 LEU A 14 -50.42 136.53
REMARK 500 1 THR A 61 -157.08 49.06
REMARK 500 1 THR A 63 166.41 153.53
REMARK 500 1 GLU A 64 -62.20 -18.14
REMARK 500 1 SER A 130 -124.59 71.48
REMARK 500 1 THR A 153 59.72 37.35
REMARK 500 1 ALA A 179 73.29 -117.84
REMARK 500 1 HIS A 184 -85.15 -115.27
REMARK 500 1 ASN A 215 -90.22 167.78
REMARK 500 1 PRO A 244 -71.02 -91.46
REMARK 500 1 ASP A 246 -173.87 73.28
REMARK 500 1 LEU A 248 133.02 146.88
REMARK 500 1 PHE A 249 94.86 -64.74
REMARK 500 1 PHE A 261 58.92 73.65
REMARK 500 2 ASN A 2 89.16 63.89
REMARK 500 2 THR A 11 -98.15 -128.60
REMARK 500 2 ASP A 12 -40.84 -157.10
REMARK 500 2 THR A 61 151.25 78.09
REMARK 500 2 GLU A 64 -29.51 -36.40
REMARK 500 2 SER A 130 -123.08 69.96
REMARK 500 2 THR A 153 58.38 36.45
REMARK 500 2 ALA A 179 71.11 -117.75
REMARK 500 2 HIS A 184 -82.84 -122.03
REMARK 500 2 ILE A 213 73.35 -166.26
REMARK 500 2 THR A 234 -46.37 -22.65
REMARK 500 2 PRO A 244 -76.20 -37.21
REMARK 500 2 ARG A 245 29.81 -152.61
REMARK 500 2 ASP A 246 145.57 90.29
REMARK 500 2 GLU A 251 -12.42 -145.50
REMARK 500 2 PHE A 261 73.16 62.57
REMARK 500 3 ASN A 2 109.97 13.72
REMARK 500 3 THR A 11 -97.36 -126.29
REMARK 500 3 ASN A 49 177.46 174.74
REMARK 500 3 THR A 61 -118.59 68.69
REMARK 500 3 THR A 63 154.98 105.34
REMARK 500 3 SER A 130 -125.45 72.28
REMARK 500 3 ASP A 176 99.86 -45.37
REMARK 500 3 HIS A 184 -83.47 -122.92
REMARK 500 3 THR A 234 -60.28 -15.10
REMARK 500 3 PRO A 244 -88.99 -16.74
REMARK 500 3 ARG A 245 45.75 -104.42
REMARK 500 3 ASP A 246 173.15 62.96
REMARK 500 3 LEU A 248 -165.45 -128.02
REMARK 500 3 PHE A 249 174.14 179.75
REMARK 500 3 GLU A 251 13.26 -142.20
REMARK 500 3 PHE A 261 49.78 80.47
REMARK 500 3 TYR A 262 77.38 26.70
REMARK 500 4 THR A 11 -80.11 -115.26
REMARK 500 4 ASP A 12 -63.50 177.56
REMARK 500 4 ASN A 48 105.48 -24.61
REMARK 500
REMARK 500 THIS ENTRY HAS 1085 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 13 LEU A 14 1 -117.14
REMARK 500 THR A 63 GLU A 64 1 142.52
REMARK 500 PRO A 214 ASN A 215 1 109.62
REMARK 500 GLY A 247 LEU A 248 1 149.42
REMARK 500 GLY A 250 GLU A 251 1 139.42
REMARK 500 ARG A 245 ASP A 246 2 146.95
REMARK 500 TYR A 262 PRO A 263 2 -149.10
REMARK 500 THR A 11 ASP A 12 3 133.66
REMARK 500 PRO A 244 ARG A 245 3 146.77
REMARK 500 GLY A 247 LEU A 248 3 140.53
REMARK 500 GLU A 251 VAL A 252 3 145.77
REMARK 500 TYR A 262 PRO A 263 3 -135.48
REMARK 500 TYR A 60 THR A 61 4 -145.90
REMARK 500 GLY A 62 THR A 63 4 -118.75
REMARK 500 ALA A 206 THR A 207 4 -146.35
REMARK 500 ARG A 245 ASP A 246 4 -138.93
REMARK 500 GLY A 247 LEU A 248 4 123.22
REMARK 500 ALA A 17 ARG A 18 5 140.81
REMARK 500 TYR A 60 THR A 61 5 -129.07
REMARK 500 THR A 61 GLY A 62 5 -141.26
REMARK 500 GLY A 62 THR A 63 5 -104.19
REMARK 500 GLY A 243 PRO A 244 5 -146.90
REMARK 500 ARG A 245 ASP A 246 5 -136.39
REMARK 500 ASP A 246 GLY A 247 5 -138.76
REMARK 500 GLY A 247 LEU A 248 5 138.30
REMARK 500 GLU A 253 GLU A 254 5 126.66
REMARK 500 ALA A 17 ARG A 18 6 143.03
REMARK 500 TYR A 60 THR A 61 6 -145.99
REMARK 500 GLY A 62 THR A 63 6 -66.18
REMARK 500 ALA A 125 VAL A 126 6 -143.82
REMARK 500 GLY A 243 PRO A 244 6 140.46
REMARK 500 ARG A 245 ASP A 246 6 -146.76
REMARK 500 LEU A 248 PHE A 249 6 -146.92
REMARK 500 PHE A 249 GLY A 250 6 -124.80
REMARK 500 GLY A 243 PRO A 244 7 -117.84
REMARK 500 GLY A 247 LEU A 248 7 140.84
REMARK 500 LEU A 248 PHE A 249 7 -148.19
REMARK 500 GLY A 243 PRO A 244 8 -124.13
REMARK 500 ARG A 245 ASP A 246 8 -127.48
REMARK 500 ALA A 17 ARG A 18 9 137.70
REMARK 500 PRO A 244 ARG A 245 9 138.32
REMARK 500 PHE A 261 TYR A 262 9 148.10
REMARK 500 GLY A 247 LEU A 248 10 146.62
REMARK 500 LEU A 248 PHE A 249 10 146.25
REMARK 500 GLY A 243 PRO A 244 11 -147.53
REMARK 500 PRO A 244 ARG A 245 11 147.48
REMARK 500 GLY A 243 PRO A 244 12 -139.34
REMARK 500 PRO A 244 ARG A 245 12 -143.97
REMARK 500 ARG A 245 ASP A 246 12 145.79
REMARK 500 ASP A 246 GLY A 247 12 -147.71
REMARK 500
REMARK 500 THIS ENTRY HAS 232 NON-CIS, NON-TRANS OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 6 GLY A 62 -14.81
REMARK 500 43 PRO A 144 -12.69
REMARK 500 46 GLN A 142 -14.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 1 ASN A 215 17.2 L L OUTSIDE RANGE
REMARK 500 4 THR A 11 25.0 L L OUTSIDE RANGE
REMARK 500 4 ASP A 246 24.8 L L OUTSIDE RANGE
REMARK 500 5 THR A 63 24.9 L L OUTSIDE RANGE
REMARK 500 5 ILE A 67 21.4 L L OUTSIDE RANGE
REMARK 500 5 ASP A 246 22.1 L L OUTSIDE RANGE
REMARK 500 6 THR A 11 23.9 L L OUTSIDE RANGE
REMARK 500 8 THR A 183 23.4 L L OUTSIDE RANGE
REMARK 500 10 TYR A 262 19.6 L L OUTSIDE RANGE
REMARK 500 11 TYR A 262 24.3 L L OUTSIDE RANGE
REMARK 500 14 ASN A 105 19.1 L L OUTSIDE RANGE
REMARK 500 15 GLU A 98 24.9 L L OUTSIDE RANGE
REMARK 500 15 GLU A 253 24.2 L L OUTSIDE RANGE
REMARK 500 22 ILE A 213 24.5 L L OUTSIDE RANGE
REMARK 500 23 ASP A 145 23.8 L L OUTSIDE RANGE
REMARK 500 26 ARG A 245 24.5 L L OUTSIDE RANGE
REMARK 500 26 PHE A 261 22.2 L L OUTSIDE RANGE
REMARK 500 27 PHE A 249 24.1 L L OUTSIDE RANGE
REMARK 500 27 TYR A 262 20.7 L L OUTSIDE RANGE
REMARK 500 28 ASN A 215 21.9 L L OUTSIDE RANGE
REMARK 500 28 TYR A 262 24.7 L L OUTSIDE RANGE
REMARK 500 29 ASN A 215 16.5 L L OUTSIDE RANGE
REMARK 500 30 PHE A 249 17.9 L L OUTSIDE RANGE
REMARK 500 30 TYR A 262 22.1 L L OUTSIDE RANGE
REMARK 500 31 PHE A 249 22.5 L L OUTSIDE RANGE
REMARK 500 31 TYR A 262 24.5 L L OUTSIDE RANGE
REMARK 500 32 ARG A 245 22.4 L L OUTSIDE RANGE
REMARK 500 33 ARG A 245 22.6 L L OUTSIDE RANGE
REMARK 500 34 PHE A 261 23.6 L L OUTSIDE RANGE
REMARK 500 35 ILE A 67 23.4 L L OUTSIDE RANGE
REMARK 500 35 ARG A 245 24.8 L L OUTSIDE RANGE
REMARK 500 35 PHE A 249 24.0 L L OUTSIDE RANGE
REMARK 500 37 ARG A 73 22.3 L L OUTSIDE RANGE
REMARK 500 37 PHE A 249 24.1 L L OUTSIDE RANGE
REMARK 500 38 ARG A 73 21.1 L L OUTSIDE RANGE
REMARK 500 40 PHE A 249 23.7 L L OUTSIDE RANGE
REMARK 500 41 ASN A 109 23.4 L L OUTSIDE RANGE
REMARK 500 41 ARG A 143 20.0 L L OUTSIDE RANGE
REMARK 500 42 ASN A 109 15.7 L L OUTSIDE RANGE
REMARK 500 43 ASN A 109 24.5 L L OUTSIDE RANGE
REMARK 500 43 ARG A 143 22.8 L L OUTSIDE RANGE
REMARK 500 43 ASN A 215 22.2 L L OUTSIDE RANGE
REMARK 500 43 LEU A 248 22.5 L L OUTSIDE RANGE
REMARK 500 44 ASN A 109 15.6 L L OUTSIDE RANGE
REMARK 500 44 TYR A 262 21.7 L L OUTSIDE RANGE
REMARK 500 46 ASN A 28 21.4 L L OUTSIDE RANGE
REMARK 500 46 ASN A 215 24.5 L L OUTSIDE RANGE
REMARK 500 47 ASN A 28 21.6 L L OUTSIDE RANGE
REMARK 500 47 ARG A 143 24.3 L L OUTSIDE RANGE
REMARK 500 47 THR A 183 24.5 L L OUTSIDE RANGE
REMARK 500
REMARK 500 THIS ENTRY HAS 88 CHIRALITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CG1 RELATED DB: PDB
REMARK 900 STRUCTURAL AND FUNCTIONAL STUDIES ON A THERMOSTABLE
REMARK 900 POLYETHYLENE TEREPHTHALATE DEGRADING HYDROLASE FROM
REMARK 900 THERMOBIFIDA FUSCA
REMARK 900 RELATED ID: 4CG2 RELATED DB: PDB
REMARK 900 STRUCTURAL AND FUNCTIONAL STUDIES ON A THERMOSTABLE
REMARK 900 POLYETHYLENE TEREPHTHALATE DEGRADING HYDROLASE FROM
REMARK 900 THERMOBIFIDA FUSCA
DBREF 4CG3 A 1 261 UNP E5BBQ3 E5BBQ3_THEFU 1 261
SEQADV 4CG3 MET A -30 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 LYS A -29 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 TYR A -28 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 LEU A -27 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 LEU A -26 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 PRO A -25 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 THR A -24 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ALA A -23 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ALA A -22 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ALA A -21 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 GLY A -20 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 LEU A -19 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 LEU A -18 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 LEU A -17 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 LEU A -16 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ALA A -15 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ALA A -14 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 GLN A -13 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 PRO A -12 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ALA A -11 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 MET A -10 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ALA A -9 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 MET A -8 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ASP A -7 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ILE A -6 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 GLY A -5 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ILE A -4 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ASN A -3 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 SER A -2 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ASP A -1 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 PRO A 0 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 TYR A 262 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 PRO A 263 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ASN A 264 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 SER A 265 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 SER A 266 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 SER A 267 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 VAL A 268 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ASP A 269 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 LYS A 270 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 LEU A 271 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ALA A 272 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ALA A 273 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 ALA A 274 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 LEU A 275 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 GLU A 276 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 HIS A 277 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 HIS A 278 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 HIS A 279 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 HIS A 280 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 HIS A 281 UNP E5BBQ3 EXPRESSION TAG
SEQADV 4CG3 HIS A 282 UNP E5BBQ3 EXPRESSION TAG
SEQRES 1 A 313 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU
SEQRES 2 A 313 LEU LEU ALA ALA GLN PRO ALA MET ALA MET ASP ILE GLY
SEQRES 3 A 313 ILE ASN SER ASP PRO ALA ASN PRO TYR GLU ARG GLY PRO
SEQRES 4 A 313 ASN PRO THR ASP ALA LEU LEU GLU ALA ARG SER GLY PRO
SEQRES 5 A 313 PHE SER VAL SER GLU GLU ASN VAL SER ARG LEU SER ALA
SEQRES 6 A 313 SER GLY PHE GLY GLY GLY THR ILE TYR TYR PRO ARG GLU
SEQRES 7 A 313 ASN ASN THR TYR GLY ALA VAL ALA ILE SER PRO GLY TYR
SEQRES 8 A 313 THR GLY THR GLU ALA SER ILE ALA TRP LEU GLY GLU ARG
SEQRES 9 A 313 ILE ALA SER HIS GLY PHE VAL VAL ILE THR ILE ASP THR
SEQRES 10 A 313 ILE THR THR LEU ASP GLN PRO ASP SER ARG ALA GLU GLN
SEQRES 11 A 313 LEU ASN ALA ALA LEU ASN HIS MET ILE ASN ARG ALA SER
SEQRES 12 A 313 SER THR VAL ARG SER ARG ILE ASP SER SER ARG LEU ALA
SEQRES 13 A 313 VAL MET GLY HIS SER MET GLY GLY GLY GLY SER LEU ARG
SEQRES 14 A 313 LEU ALA SER GLN ARG PRO ASP LEU LYS ALA ALA ILE PRO
SEQRES 15 A 313 LEU THR PRO TRP HIS LEU ASN LYS ASN TRP SER SER VAL
SEQRES 16 A 313 THR VAL PRO THR LEU ILE ILE GLY ALA ASP LEU ASP THR
SEQRES 17 A 313 ILE ALA PRO VAL ALA THR HIS ALA LYS PRO PHE TYR ASN
SEQRES 18 A 313 SER LEU PRO SER SER ILE SER LYS ALA TYR LEU GLU LEU
SEQRES 19 A 313 ASP GLY ALA THR HIS PHE ALA PRO ASN ILE PRO ASN LYS
SEQRES 20 A 313 ILE ILE GLY LYS TYR SER VAL ALA TRP LEU LYS ARG PHE
SEQRES 21 A 313 VAL ASP ASN ASP THR ARG TYR THR GLN PHE LEU CYS PRO
SEQRES 22 A 313 GLY PRO ARG ASP GLY LEU PHE GLY GLU VAL GLU GLU TYR
SEQRES 23 A 313 ARG SER THR CYS PRO PHE TYR PRO ASN SER SER SER VAL
SEQRES 24 A 313 ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS
SEQRES 25 A 313 HIS
HET SO4 A1001 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *99(H2 O)
HELIX 1 1 THR A 63 SER A 76 1 14
HELIX 2 2 GLN A 92 ARG A 110 1 19
HELIX 3 3 SER A 112 SER A 117 1 6
HELIX 4 4 SER A 130 SER A 141 1 12
HELIX 5 5 HIS A 184 LEU A 192 1 9
HELIX 6 6 ASN A 215 ASP A 231 1 17
HELIX 7 7 ASP A 233 ARG A 235 5 3
HELIX 8 8 TYR A 236 CYS A 241 1 6
SHEET 1 AA 6 VAL A 24 VAL A 29 0
SHEET 2 AA 6 GLY A 40 PRO A 45 -1 O GLY A 40 N VAL A 29
SHEET 3 AA 6 VAL A 80 ILE A 84 -1 O VAL A 81 N TYR A 43
SHEET 4 AA 6 TYR A 51 SER A 57 1 O GLY A 52 N VAL A 80
SHEET 5 AA 6 ILE A 119 HIS A 129 1 N ASP A 120 O TYR A 51
SHEET 6 AA 6 ALA A 148 LEU A 152 1 O ALA A 148 N VAL A 126
SHEET 1 AB 3 THR A 168 ALA A 173 0
SHEET 2 AB 3 LYS A 198 LEU A 203 1 O ALA A 199 N ILE A 170
SHEET 3 AB 3 VAL A 252 SER A 257 -1 N GLU A 253 O GLU A 202
SSBOND 1 CYS A 241 CYS A 259 1555 1555 2.05
CISPEP 1 CYS A 241 PRO A 242 1 5.94
CISPEP 2 CYS A 259 PRO A 260 1 15.50
CISPEP 3 CYS A 241 PRO A 242 2 3.05
CISPEP 4 CYS A 259 PRO A 260 2 15.42
CISPEP 5 CYS A 241 PRO A 242 3 5.77
CISPEP 6 CYS A 259 PRO A 260 3 12.45
CISPEP 7 CYS A 241 PRO A 242 4 10.07
CISPEP 8 CYS A 259 PRO A 260 4 16.88
CISPEP 9 CYS A 241 PRO A 242 5 5.73
CISPEP 10 CYS A 259 PRO A 260 5 12.94
CISPEP 11 CYS A 241 PRO A 242 6 7.85
CISPEP 12 CYS A 259 PRO A 260 6 16.57
CISPEP 13 CYS A 241 PRO A 242 7 4.83
CISPEP 14 CYS A 259 PRO A 260 7 16.27
CISPEP 15 CYS A 241 PRO A 242 8 5.02
CISPEP 16 CYS A 259 PRO A 260 8 16.77
CISPEP 17 CYS A 241 PRO A 242 9 11.69
CISPEP 18 CYS A 259 PRO A 260 9 14.59
CISPEP 19 CYS A 241 PRO A 242 10 9.59
CISPEP 20 CYS A 259 PRO A 260 10 11.77
CISPEP 21 CYS A 241 PRO A 242 11 6.59
CISPEP 22 CYS A 259 PRO A 260 11 13.21
CISPEP 23 CYS A 241 PRO A 242 12 7.52
CISPEP 24 CYS A 259 PRO A 260 12 19.71
CISPEP 25 CYS A 241 PRO A 242 13 5.07
CISPEP 26 CYS A 259 PRO A 260 13 14.36
CISPEP 27 CYS A 241 PRO A 242 14 5.42
CISPEP 28 CYS A 259 PRO A 260 14 15.72
CISPEP 29 CYS A 241 PRO A 242 15 7.38
CISPEP 30 CYS A 259 PRO A 260 15 15.64
CISPEP 31 CYS A 241 PRO A 242 16 6.32
CISPEP 32 CYS A 259 PRO A 260 16 12.96
CISPEP 33 CYS A 241 PRO A 242 17 4.97
CISPEP 34 CYS A 259 PRO A 260 17 14.48
CISPEP 35 CYS A 241 PRO A 242 18 8.24
CISPEP 36 CYS A 259 PRO A 260 18 14.82
CISPEP 37 CYS A 241 PRO A 242 19 6.37
CISPEP 38 CYS A 259 PRO A 260 19 14.95
CISPEP 39 CYS A 241 PRO A 242 20 7.42
CISPEP 40 CYS A 259 PRO A 260 20 14.91
CISPEP 41 CYS A 241 PRO A 242 21 5.12
CISPEP 42 CYS A 259 PRO A 260 21 14.99
CISPEP 43 CYS A 241 PRO A 242 22 3.84
CISPEP 44 CYS A 259 PRO A 260 22 16.51
CISPEP 45 CYS A 241 PRO A 242 23 6.34
CISPEP 46 CYS A 259 PRO A 260 23 15.09
CISPEP 47 CYS A 241 PRO A 242 24 8.25
CISPEP 48 CYS A 259 PRO A 260 24 14.15
CISPEP 49 CYS A 241 PRO A 242 25 6.50
CISPEP 50 CYS A 259 PRO A 260 25 16.14
CISPEP 51 CYS A 241 PRO A 242 26 5.17
CISPEP 52 CYS A 259 PRO A 260 26 16.34
CISPEP 53 CYS A 241 PRO A 242 27 6.97
CISPEP 54 CYS A 259 PRO A 260 27 11.14
CISPEP 55 CYS A 241 PRO A 242 28 8.24
CISPEP 56 CYS A 259 PRO A 260 28 15.55
CISPEP 57 CYS A 241 PRO A 242 29 5.15
CISPEP 58 CYS A 259 PRO A 260 29 17.62
CISPEP 59 CYS A 241 PRO A 242 30 6.12
CISPEP 60 CYS A 259 PRO A 260 30 16.34
CISPEP 61 CYS A 241 PRO A 242 31 5.30
CISPEP 62 CYS A 259 PRO A 260 31 14.50
CISPEP 63 CYS A 241 PRO A 242 32 5.80
CISPEP 64 CYS A 259 PRO A 260 32 13.60
CISPEP 65 CYS A 241 PRO A 242 33 6.58
CISPEP 66 CYS A 259 PRO A 260 33 13.46
CISPEP 67 CYS A 241 PRO A 242 34 6.03
CISPEP 68 CYS A 259 PRO A 260 34 10.12
CISPEP 69 CYS A 241 PRO A 242 35 8.39
CISPEP 70 CYS A 259 PRO A 260 35 20.07
CISPEP 71 CYS A 241 PRO A 242 36 5.61
CISPEP 72 CYS A 259 PRO A 260 36 15.65
CISPEP 73 CYS A 241 PRO A 242 37 5.19
CISPEP 74 CYS A 259 PRO A 260 37 14.03
CISPEP 75 CYS A 241 PRO A 242 38 9.73
CISPEP 76 CYS A 259 PRO A 260 38 13.09
CISPEP 77 CYS A 241 PRO A 242 39 6.47
CISPEP 78 CYS A 259 PRO A 260 39 16.77
CISPEP 79 CYS A 241 PRO A 242 40 6.83
CISPEP 80 CYS A 259 PRO A 260 40 15.55
CISPEP 81 CYS A 241 PRO A 242 41 7.86
CISPEP 82 CYS A 259 PRO A 260 41 16.42
CISPEP 83 CYS A 241 PRO A 242 42 7.28
CISPEP 84 CYS A 259 PRO A 260 42 17.16
CISPEP 85 CYS A 241 PRO A 242 43 7.05
CISPEP 86 CYS A 259 PRO A 260 43 10.39
CISPEP 87 CYS A 241 PRO A 242 44 8.25
CISPEP 88 CYS A 259 PRO A 260 44 18.73
CISPEP 89 CYS A 241 PRO A 242 45 7.70
CISPEP 90 CYS A 259 PRO A 260 45 14.04
CISPEP 91 CYS A 241 PRO A 242 46 7.51
CISPEP 92 CYS A 259 PRO A 260 46 14.91
CISPEP 93 CYS A 241 PRO A 242 47 5.45
CISPEP 94 CYS A 259 PRO A 260 47 14.81
CISPEP 95 CYS A 241 PRO A 242 48 8.44
CISPEP 96 CYS A 259 PRO A 260 48 17.57
CISPEP 97 CYS A 241 PRO A 242 49 1.97
CISPEP 98 CYS A 259 PRO A 260 49 14.06
CISPEP 99 CYS A 241 PRO A 242 50 5.29
CISPEP 100 CYS A 259 PRO A 260 50 12.60
CISPEP 101 CYS A 241 PRO A 242 51 5.17
CISPEP 102 CYS A 259 PRO A 260 51 15.41
CISPEP 103 CYS A 241 PRO A 242 52 4.76
CISPEP 104 CYS A 259 PRO A 260 52 15.05
CISPEP 105 CYS A 241 PRO A 242 53 6.69
CISPEP 106 CYS A 259 PRO A 260 53 14.13
CISPEP 107 CYS A 241 PRO A 242 54 7.10
CISPEP 108 CYS A 259 PRO A 260 54 15.86
CISPEP 109 CYS A 241 PRO A 242 55 6.47
CISPEP 110 CYS A 259 PRO A 260 55 13.02
CISPEP 111 CYS A 241 PRO A 242 56 6.41
CISPEP 112 CYS A 259 PRO A 260 56 13.48
CISPEP 113 CYS A 241 PRO A 242 57 6.03
CISPEP 114 CYS A 259 PRO A 260 57 18.39
CISPEP 115 CYS A 241 PRO A 242 58 5.83
CISPEP 116 CYS A 259 PRO A 260 58 12.71
CISPEP 117 CYS A 241 PRO A 242 59 6.55
CISPEP 118 CYS A 259 PRO A 260 59 15.41
CISPEP 119 CYS A 241 PRO A 242 60 6.66
CISPEP 120 CYS A 259 PRO A 260 60 17.07
CISPEP 121 CYS A 241 PRO A 242 61 6.72
CISPEP 122 CYS A 259 PRO A 260 61 14.19
CISPEP 123 CYS A 241 PRO A 242 62 5.32
CISPEP 124 CYS A 259 PRO A 260 62 13.23
CISPEP 125 CYS A 241 PRO A 242 63 6.75
CISPEP 126 CYS A 259 PRO A 260 63 12.51
CISPEP 127 CYS A 241 PRO A 242 64 4.89
CISPEP 128 CYS A 259 PRO A 260 64 9.00
CISPEP 129 CYS A 241 PRO A 242 65 2.99
CISPEP 130 CYS A 259 PRO A 260 65 15.60
CISPEP 131 CYS A 241 PRO A 242 66 5.69
CISPEP 132 CYS A 259 PRO A 260 66 15.74
CISPEP 133 CYS A 241 PRO A 242 67 8.03
CISPEP 134 CYS A 259 PRO A 260 67 13.92
CISPEP 135 CYS A 241 PRO A 242 68 4.93
CISPEP 136 CYS A 259 PRO A 260 68 15.13
CISPEP 137 CYS A 241 PRO A 242 69 6.08
CISPEP 138 CYS A 259 PRO A 260 69 14.26
CISPEP 139 CYS A 241 PRO A 242 70 6.12
CISPEP 140 CYS A 259 PRO A 260 70 18.11
CISPEP 141 CYS A 241 PRO A 242 71 5.77
CISPEP 142 CYS A 259 PRO A 260 71 12.98
CISPEP 143 CYS A 241 PRO A 242 72 6.55
CISPEP 144 CYS A 259 PRO A 260 72 11.04
CISPEP 145 CYS A 241 PRO A 242 73 5.47
CISPEP 146 CYS A 259 PRO A 260 73 15.31
CISPEP 147 CYS A 241 PRO A 242 74 4.73
CISPEP 148 CYS A 259 PRO A 260 74 16.71
CISPEP 149 CYS A 241 PRO A 242 75 4.89
CISPEP 150 CYS A 259 PRO A 260 75 14.36
CISPEP 151 CYS A 241 PRO A 242 76 8.98
CISPEP 152 CYS A 259 PRO A 260 76 13.71
CISPEP 153 CYS A 241 PRO A 242 77 6.44
CISPEP 154 CYS A 259 PRO A 260 77 11.11
SITE 1 AC1 5 VAL A 24 ARG A 46 ARG A 256 SER A 257
SITE 2 AC1 5 HOH A1160
CRYST1 117.900 117.900 36.440 90.00 90.00 90.00 I 41 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008482 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008482 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027442 0.00000
MODEL 1
TER 3981 PRO A 263
ENDMDL
MODEL 2
TER 3981 PRO A 263
ENDMDL
MODEL 3
TER 3981 PRO A 263
ENDMDL
MODEL 4
TER 3981 PRO A 263
ENDMDL
MODEL 5
TER 3981 PRO A 263
ENDMDL
MODEL 6
TER 3981 PRO A 263
ENDMDL
MODEL 7
TER 3981 PRO A 263
ENDMDL
MODEL 8
TER 3981 PRO A 263
ENDMDL
MODEL 9
TER 3981 PRO A 263
ENDMDL
MODEL 10
TER 3981 PRO A 263
ENDMDL
MODEL 11
TER 3981 PRO A 263
ENDMDL
MODEL 12
TER 3981 PRO A 263
ENDMDL
MODEL 13
TER 3981 PRO A 263
ENDMDL
MODEL 14
TER 3981 PRO A 263
ENDMDL
MODEL 15
TER 3981 PRO A 263
ENDMDL
MODEL 16
TER 3981 PRO A 263
ENDMDL
MODEL 17
TER 3981 PRO A 263
ENDMDL
MODEL 18
TER 3981 PRO A 263
ENDMDL
MODEL 19
TER 3981 PRO A 263
ENDMDL
MODEL 20
TER 3981 PRO A 263
ENDMDL
MODEL 21
TER 3981 PRO A 263
ENDMDL
MODEL 22
TER 3981 PRO A 263
ENDMDL
MODEL 23
TER 3981 PRO A 263
ENDMDL
MODEL 24
TER 3981 PRO A 263
ENDMDL
MODEL 25
TER 3981 PRO A 263
ENDMDL
MODEL 26
TER 3981 PRO A 263
ENDMDL
MODEL 27
TER 3981 PRO A 263
ENDMDL
MODEL 28
TER 3981 PRO A 263
ENDMDL
MODEL 29
TER 3981 PRO A 263
ENDMDL
MODEL 30
TER 3981 PRO A 263
ENDMDL
MODEL 31
TER 3981 PRO A 263
ENDMDL
MODEL 32
TER 3981 PRO A 263
ENDMDL
MODEL 33
TER 3981 PRO A 263
ENDMDL
MODEL 34
TER 3981 PRO A 263
ENDMDL
MODEL 35
TER 3981 PRO A 263
ENDMDL
MODEL 36
TER 3981 PRO A 263
ENDMDL
MODEL 37
TER 3981 PRO A 263
ENDMDL
MODEL 38
TER 3981 PRO A 263
ENDMDL
MODEL 39
TER 3981 PRO A 263
ENDMDL
MODEL 40
TER 3981 PRO A 263
ENDMDL
MODEL 41
TER 3981 PRO A 263
ENDMDL
MODEL 42
TER 3981 PRO A 263
ENDMDL
MODEL 43
TER 3981 PRO A 263
ENDMDL
MODEL 44
TER 3981 PRO A 263
ENDMDL
MODEL 45
TER 3981 PRO A 263
ENDMDL
MODEL 46
TER 3981 PRO A 263
ENDMDL
MODEL 47
TER 3981 PRO A 263
ENDMDL
MODEL 48
TER 3981 PRO A 263
ENDMDL
MODEL 49
TER 3981 PRO A 263
ENDMDL
MODEL 50
TER 3981 PRO A 263
ENDMDL
MODEL 51
TER 3981 PRO A 263
ENDMDL
MODEL 52
TER 3981 PRO A 263
ENDMDL
MODEL 53
TER 3981 PRO A 263
ENDMDL
MODEL 54
TER 3981 PRO A 263
ENDMDL
MODEL 55
TER 3981 PRO A 263
ENDMDL
MODEL 56
TER 3981 PRO A 263
ENDMDL
MODEL 57
TER 3981 PRO A 263
ENDMDL
MODEL 58
TER 3981 PRO A 263
ENDMDL
MODEL 59
TER 3981 PRO A 263
ENDMDL
MODEL 60
TER 3981 PRO A 263
ENDMDL
MODEL 61
TER 3981 PRO A 263
ENDMDL
MODEL 62
TER 3981 PRO A 263
ENDMDL
MODEL 63
TER 3981 PRO A 263
ENDMDL
MODEL 64
TER 3981 PRO A 263
ENDMDL
MODEL 65
TER 3981 PRO A 263
ENDMDL
MODEL 66
TER 3981 PRO A 263
ENDMDL
MODEL 67
TER 3981 PRO A 263
ENDMDL
MODEL 68
TER 3981 PRO A 263
ENDMDL
MODEL 69
TER 3981 PRO A 263
ENDMDL
MODEL 70
TER 3981 PRO A 263
ENDMDL
MODEL 71
TER 3981 PRO A 263
ENDMDL
MODEL 72
TER 3981 PRO A 263
ENDMDL
MODEL 73
TER 3981 PRO A 263
ENDMDL
MODEL 74
TER 3981 PRO A 263
ENDMDL
MODEL 75
TER 3981 PRO A 263
ENDMDL
MODEL 76
TER 3981 PRO A 263
ENDMDL
MODEL 77
TER 3981 PRO A 263
ENDMDL
MASTER 691 0 1 8 9 0 2 6 4084 77 7 25
END |